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Literature summary for 2.5.1.19 extracted from

  • Mizyed, S.; Wright, J.E.; Byczynski, B.; Berti, P.J.
    Identification of the catalytic residues of AroA (Enolpyruvylshikimate 3-phosphate synthase) using partitioning analysis (2003), Biochemistry, 42, 6986-6995.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type, His-tagged wild-type and several mutant enzymes in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
D313A 0.42% of wild-type activity Escherichia coli
D313N 5% of wild-type activity Escherichia coli
D49A 41% of wild-type activity Escherichia coli
E341A 0.3% of wild-type activity Escherichia coli
E341Q 10% of wild-type activity Escherichia coli
H385A 0.08% of wild-type activity Escherichia coli
K22A 0.7% of wild-type activity Escherichia coli
K22R 3% of wild-type activity Escherichia coli
K340A 2.4% of wild-type activity Escherichia coli
K411A 10.4% of wild-type activity Escherichia coli
N94A 50% of wild-type activity Escherichia coli
Q171A 1.7% of wild-type activity Escherichia coli
R100M 0.2% of wild-type activity Escherichia coli
R124A 19.6% of wild-type activity Escherichia coli
R344K 31.7% of wild-type activity Escherichia coli
R344M 16.3% of wild-type activity Escherichia coli
R386M 15.8% of wild-type activity Escherichia coli
Y200F 1% of wild-type activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6D3
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20
-
recombinant His-tagged wild-type enzyme Escherichia coli
24
-
recombinant wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + 3-phosphoshikimate
-
Escherichia coli phosphate + 5-enolpyruvylshikimate 3-phosphate
-
r